{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T17:15:20Z","timestamp":1777396520623,"version":"3.51.4"},"reference-count":36,"publisher":"SAGE Publications","issue":"2","license":[{"start":{"date-parts":[[2024,5,14]],"date-time":"2024-05-14T00:00:00Z","timestamp":1715644800000},"content-version":"unspecified","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["JAD"],"published-print":{"date-parts":[[2024,5,14]]},"abstract":"<jats:p>Background: Amyloid-\u03b2 (A\u03b2) is one of the hallmark lesions of Alzheimer\u2019s disease (AD). During the disease process, A\u03b2 undergoes biochemical changes, producing toxic A\u03b2 variants, proposed to be detected within the neurons. Idiopathic normal pressure hydrocephalus (iNPH) causes cognitive impairment, gait, and urinary symptoms in elderly, that can be reversed by a ventriculo-peritoneal shunt. Majority of iNPH subjects display different A\u03b2 variants in their brain biopsies, obtained during shunting. Objective: To study the cellular compartmentalization of different A\u03b2 variants in brain biopsies from iNPH subjects. Methods: We studied the cellular localization of different proteoforms of A\u03b2 using antibodies towards different amino acid sequences or post-translational modifications of A\u03b2, including clones 4G8, 6F\/3D, unmodified- (7H3D6), pyroglutamylated- (N3pE), phosphorylated-(1E4E11) A\u03b2 and A\u03b2 protein precursor (A\u03b2PP), in brain biopsies from 3 iNPH subjects, using immunohistochemistry and light microscopy (LM), light microscopy on semi-thin sections (LMst), and electron microscopy (EM). Results: In LM all A\u03b2 variants were detected. In LMst and EM, the A\u03b2 4G8, 6F\/3D, and the pyroglutamylated A\u03b2 were detected. The A\u03b2PP was visualized by all methods. The A\u03b2 labelling was located extracellularly with no specific signal within the intracellular compartment, whereas the A\u03b2PP was seen both intra- and extracellularly. Conclusions: The A\u03b2 markers displayed extracellular localization when visualized by three assessment techniques, reflecting the pathological extracellular accumulation of A\u03b2 in the human brain. No intracellular A\u03b2 pathology was seen. A\u03b2PP was visualized in intra- and extracellularly, which corresponds to the localization of the protein in the membranes of cells and organelles.<\/jats:p>","DOI":"10.3233\/jad-240167","type":"journal-article","created":{"date-parts":[[2024,4,26]],"date-time":"2024-04-26T14:05:27Z","timestamp":1714140327000},"page":"729-737","source":"Crossref","is-referenced-by-count":0,"title":["The Compartmentalization of Amyloid-\u03b2 in Idiopathic Normal Pressure Hydrocephalus Brain Biopsies"],"prefix":"10.1177","volume":"99","author":[{"given":"Sylwia","family":"Libard","sequence":"first","affiliation":[{"name":"Department of Pathology, Uppsala University Hospital, Uppsala, Sweden"},{"name":"Department of Immunology, Genetics and Pathology, Uppsala University, Uppsala, Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Monika","family":"Hodik","sequence":"additional","affiliation":[{"name":"Department of Immunology, Genetics and Pathology, Uppsala University, Uppsala, 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